EP0346137B1 - Enzymatic dishwashing composition - Google Patents
Enzymatic dishwashing composition Download PDFInfo
- Publication number
- EP0346137B1 EP0346137B1 EP89305836A EP89305836A EP0346137B1 EP 0346137 B1 EP0346137 B1 EP 0346137B1 EP 89305836 A EP89305836 A EP 89305836A EP 89305836 A EP89305836 A EP 89305836A EP 0346137 B1 EP0346137 B1 EP 0346137B1
- Authority
- EP
- European Patent Office
- Prior art keywords
- lipase
- composition according
- lipases
- dishwashing
- chlorinated
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Lifetime
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Classifications
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
- C11D3/38627—Preparations containing enzymes, e.g. protease or amylase containing lipase
Definitions
- the present invention relates to an enzymatic dishwashing composition
- a chlorine-type bleaching agent comprising a chlorine-type bleaching agent, and is characterised by the use of lipase as further described below, and a process of (e.g. mechanical) dishwashing using such a composition.
- lipases as a general class of enzymes have also been suggested, no specific proposals relating to the use of lipases in dishwashing compositions have been made as far as we know.
- dishwashing compositions contain a chlorine-type bleaching agent, and it is well known in the art that, on the whole, enzymes are not really compatible with such chlorine-type bleaching agents.
- lipases in compositions which contain a chlorine-type bleaching agent in a non-protected form are surprisingly more stable and do not lose their activity as rapidly as one would have expected.
- the present invention therefore relates to an enzymatic dishwashing composition
- a detergent-active material comprising a lipase and a chlorine-type agent.
- the lipases used according to the present invention, may be of any suitable origin such as yeasts, fungi and bacteria. Preferably they are of bacterial or fungal origin.
- the bacterial lipases belong to the class of bacterial lipases which show a positive immunological cross-reaction with antibody raised against the lipase produced by the microorganism Chromobacter viscosum var. lipolyticum NRRL B-3763.
- This lipase has been described in Dutch Patent Specification 154,269 of Toyo Jozo, and the microorganism is available to the public at the United States Department of Agriculture, Agricultural Research Service, Northern Utilisation and Development Division at Peoria, Illinois, under the number NRRL B-3673.
- This lipase will hereinafter be referred to as "Toyo Jozo" lipase.
- the preferred bacterial lipases of the present invention should show a positive immunological cross-reaction with the Toyo Jozo lipase antibody, using the standard and well-known immunodiffusion procedure according to Ouchterlony (Acta. Med. Scan., 133 , pages 76-79 (1950)).
- the preparation of the antiserum is carried out as follows: Equal volumes of 0.1 mg/ml antigen and of Freund's adjuvant (complete or incomplete) are mixed until an emulsion is obtained. Two female rabbits are injected with 2 ml samples of the emulsion according to the following scheme:
- the serum containing the required antibody is prepared by centrifugation of clotted blood, taken on day 67.
- the titre of the anti-Toyo Jozo-lipase antiserum is determined by the inspection of precipitation of serial dilutions of antigen and antiserum according to the Ouchterlony procedure. A 25 dilution of antiserum was the dilution that still gave a visible precipitation with an antigen concentration of 0.1 mg/ml.
- All bacterial lipases showing a positive immunological cross reaction with the Toyo Jozo lipase antibody as hereabove described are preferred bacterial lipases according to the present invention.
- Typical examples thereof are the lipases ex Pseudomonas fluorescens IAM 1057 (available under the trade name Amano-P), the lipase ex Pseudomonas fragi FERM P 1339 (available under the trade name Amano-B), lipase ex Pseudomonas nitroreducens var. lipolyticum FERM P 1338, the lipase ex Pseudomonas sp.
- lipases ex Chromobacter viscosum , e.g. Chromobacter viscosum var. lipolyticum NRRLB 3673, commercially available from Toyo Jozo Co., Tagata, Japan; and further Chromobacter viscosum lipases from US Biochemical Corp, U.S.A. and Diosynth Co., The Netherlands, and lipases ex Pseudomonas gladioli .
- Suitable fungal lipases which may also be used in the present invention are lipases ex Humicola lanuginosa or Thermomyces lanuginosus , such as Amano-CE ex Amano or those described in the published European Patent Application 0 258 068 (Novo), (incorporated herein by reference).
- Lipases particularly preferred to be used in the present invention are the lipases produced by cloning, by rDNA technologies, the gene encoding for the lipase produced by the fungus Humicola lanuginosa and expressing the gene in Aspergillus oryzae as host.
- a lipase is manufactured and sold by Novo Industri A/S, Denmark, under the trade name Lipolase (described in Biotechnology Newswatch, 7th March 1988, page 6), and further such lipases are made in accordance with EP 0 305 216 (NOVO), (incorporated herein by reference).
- the lipases of the present invention are included in the detergent composition in such an amount that the final detergent composition has a lipolytic enzyme activity of from 100 to 0.005 LU/mg preferably 25 to 0.05 LU/mg of the composition.
- lipases can be used in their nonpurified form, or in a purified form, e.g. purified with the aid of well-known adsorption methods, such as a phenylsepharose-adsorption techniques.
- compositions further comprise a chlorine-type bleaching agent, generally in an amount corresponding to 0.1-15%, usually 0.5-10% by weight of available chlorine.
- chlorine-type bleaching agents organic and/or inorganic compounds are meant, which yield, on solution in water, active chlorine.
- Typical examples are alkali metal hypochlorites, chlorinated trisodium phosphate, chlorinated (sulphon) amides, chlorinated hydantoins, chlorinated cyanuric acids and salts (usually alkali metal, e.g. sodium, salts) thereof, etc.
- compositions also contain a detergent-active compound, generally in an amount of from 0.5-10%, usually 1-5%.
- a detergent-active compound such as soaps, synthetic anionic, non-ionic, amphoteric detergent surfactant and mixtures thereof.
- a nonionic detergent surfactant is used, especially a low-foaming one. Suitable examples of such nonionic detergent surfactants can easily be found in M Schick "Nonionic Surfactants" (1967).
- the composition of the invention may furthermore comprise the usual ingredients of dishwashing or rinse compositions.
- it may contain one or more alkali salts commonly used in dishwashing compositions.
- it may contain organic and/or inorganic builders such as the alkali metal ortho-, pyro and tripolyphosphates and hexametaphosphates, silicates, carbonates, zeolites, borates, citrates, carboxymethyloxysuccinates, nitrilotriacetates and ethylenediamine-tetraacetates, polymeric polyelectrolytes such as polyacrylates, polymaleates, and other known organic and inorganic builder compounds.
- Caustic alkali e.g. NAOH
- the compositions often generate a pH >10 on dissolution/dispersion at a surfactant level in the range of 0.4 - 0.8 g/l.
- the amount of builders in the composition varies from 10-90% by weight, generally from 30-70% by weight.
- the composition may furthermore contain other useful additives such as oxygen-type bleaching agents such as perborate, reducing bleaching agents such as sodium sulphite, bleaching agent activators, hydrotropes, fillers, perfumes, colouring agents, germicides, soil-suspending agents, aminopoly-phosphonic acids and alkali metal or alkaline earth metal salts thereof, clays such as hectorites, anti-corrosion agents such as fatty acids, benztriazole and so on.
- Other enzymes such as proteases, e.g. Savinase R ex Novo, amylases, e.g. Termamyl R ex Novo, and oxidases may also be included.
- the dishwashing compositions of the invention may contain proteases in such an amount, that the final composition has a proteolytic activity of 0.1-50, usually 1-50 and preferably 5-30 GU/mg.
- a GU is a glycine unit, which is the amount of enzyme which under standard incubation conditions produces an amount of terminal NH2-groups equivalent to 1 microgram/ml glycine.
- the preferred proteases are those of the subtilisen type (e.g. the Savinase preparation mentioned above), but it is preferred that the lipase preparation is itself substantially free of accompanying protease, e.g. less than about 0.3 GU per lipase unit, preferably not more than about 0.15 GU per lipase unit.
- amylases When amylases are present, they are used in such amounts that the final composition has an amylolytic activity of 103-107 MU/kg of final product.
- a maltose unit (MU) is determined by the method as described in P Bernfeld in “Methods in Enzymology", Vol I, (1955), page 149.
- a typical example of a machine dishwashing composition contains a lipase in an amount as set out above, an alkali metal tripolyphosphate in an amount of from 20-60%, an alkali metal silicate in an amount of from 40-80%, or an alkali metal disilicate in an amount of 5-30% by weight, a chlorine-type bleaching agent such as dichlorocyanuric acid (sodium or potassium salt) in an amount of from 0.5-10%, a low-foaming detergent surfactant in an amount of from 0.5-5%, and minor ingredients such as perfumes, colouring agents, hydrotropes, fillers, etc.
- a lipase in an amount as set out above
- an alkali metal tripolyphosphate in an amount of from 20-60%
- an alkali metal silicate in an amount of from 40-80%
- an alkali metal disilicate in an amount of 5-30% by weight
- a chlorine-type bleaching agent such as dichlorocyanuric acid (sodium or
- the products of the invention can be formulated in any desirable form, such as powders, granulates, cakes, bars, pastes, liquids etc.
- the proportions given above are (wherever appropriate) expressed in terms of the dry weight.
- composition B of Example 1 With composition B of Example 1, the same test was repeated (at pH 10.9) with Lipolase, or the lipase ex Pseudomonas cepacia or the lipase ex Humicola lanuginosa according to European Patent Application 0 258 068, all dosed at 15 LU/ml.
- the lipolase enzyme (highly preferred) is free of protease of fungal origin, while the Lipase obtained directly from Humicola lanuginosa had some fungal protease therein, (probably more than 0.3 GU per Lipase unit).
- the dishwashing composition was dosed in an amount of 3 g/l, and had the following formulation: % by weight sodium tripolyphosphate 24.0 soda ash 20.0 sodium disilicate 11.0 linear C10 alcohol, condensed with 6 moles of ethylene oxide and 24 moles of propylene oxide 2.5 sodium sulphate 44.0 sodium dichlorocyanuric acid salt 1.2 water to 100.0
- the load was a dummy load without soil, and the soiling was 35 g/run fresh egg-yolk.
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- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- Wood Science & Technology (AREA)
- Organic Chemistry (AREA)
- Detergent Compositions (AREA)
- Enzymes And Modification Thereof (AREA)
Description
- The present invention relates to an enzymatic dishwashing composition comprising a chlorine-type bleaching agent, and is characterised by the use of lipase as further described below, and a process of (e.g. mechanical) dishwashing using such a composition.
- The use of enzymes in dishwashing compositions, both for manual as well as mechanical dishwashing, is generally well known in the art. For that purpose in particular amylases and/or proteases have been proposed.
- Although lipases as a general class of enzymes have also been suggested, no specific proposals relating to the use of lipases in dishwashing compositions have been made as far as we know.
- Many dishwashing compositions contain a chlorine-type bleaching agent, and it is well known in the art that, on the whole, enzymes are not really compatible with such chlorine-type bleaching agents.
- We have now surprisingly found that lipases in compositions which contain a chlorine-type bleaching agent in a non-protected form are surprisingly more stable and do not lose their activity as rapidly as one would have expected.
- In addition, we have surprisingly found that less spot formation occurs when using the compositions of the invention, compared with a composition with a chlorine-type bleaching agent but without a lipase.
- The present invention therefore relates to an enzymatic dishwashing composition comprising a detergent-active material, a lipase and a chlorine-type agent.
- The lipases, used according to the present invention, may be of any suitable origin such as yeasts, fungi and bacteria. Preferably they are of bacterial or fungal origin. The bacterial lipases belong to the class of bacterial lipases which show a positive immunological cross-reaction with antibody raised against the lipase produced by the microorganism Chromobacter viscosum var. lipolyticum NRRL B-3763.
- This lipase has been described in Dutch Patent Specification 154,269 of Toyo Jozo, and the microorganism is available to the public at the United States Department of Agriculture, Agricultural Research Service, Northern Utilisation and Development Division at Peoria, Illinois, under the number NRRL B-3673. This lipase will hereinafter be referred to as "Toyo Jozo" lipase. The preferred bacterial lipases of the present invention should show a positive immunological cross-reaction with the Toyo Jozo lipase antibody, using the standard and well-known immunodiffusion procedure according to Ouchterlony (Acta. Med. Scan., 133, pages 76-79 (1950)).
- The preparation of the antiserum is carried out as follows:
Equal volumes of 0.1 mg/ml antigen and of Freund's adjuvant (complete or incomplete) are mixed until an emulsion is obtained. Two female rabbits are injected with 2 ml samples of the emulsion according to the following scheme: - Day 0
- : antigen in complete Freund's adjuvant
- Day 4
- : antigen in complete Freund's adjuvant
- Day 32
- : antigen in incomplete Freund's adjuvant
- Day 60
- : booster of antigen in incomplete Freund's adjuvant.
- The serum containing the required antibody is prepared by centrifugation of clotted blood, taken on day 67.
- The titre of the anti-Toyo Jozo-lipase antiserum is determined by the inspection of precipitation of serial dilutions of antigen and antiserum according to the Ouchterlony procedure. A 2⁵ dilution of antiserum was the dilution that still gave a visible precipitation with an antigen concentration of 0.1 mg/ml.
- All bacterial lipases showing a positive immunological cross reaction with the Toyo Jozo lipase antibody as hereabove described are preferred bacterial lipases according to the present invention. Typical examples thereof are the lipases ex Pseudomonas fluorescens IAM 1057 (available under the trade name Amano-P), the lipase ex Pseudomonas fragi FERM P 1339 (available under the trade name Amano-B), lipase ex Pseudomonas nitroreducens var. lipolyticum FERM P 1338, the lipase ex Pseudomonas sp. available under the trade name Amano-CES, the lipase ex Pseudomonas cepacia, lipases ex Chromobacter viscosum, e.g. Chromobacter viscosum var. lipolyticum NRRLB 3673, commercially available from Toyo Jozo Co., Tagata, Japan; and further Chromobacter viscosum lipases from US Biochemical Corp, U.S.A. and Diosynth Co., The Netherlands, and lipases ex Pseudomonas gladioli.
- Suitable fungal lipases which may also be used in the present invention are lipases ex Humicola lanuginosa or Thermomyces lanuginosus, such as Amano-CE ex Amano or those described in the published European Patent Application 0 258 068 (Novo), (incorporated herein by reference).
- Lipases particularly preferred to be used in the present invention are the lipases produced by cloning, by rDNA technologies, the gene encoding for the lipase produced by the fungus Humicola lanuginosa and expressing the gene in Aspergillus oryzae as host. Such a lipase is manufactured and sold by Novo Industri A/S, Denmark, under the trade name Lipolase (described in Biotechnology Newswatch, 7th March 1988, page 6), and further such lipases are made in accordance with EP 0 305 216 (NOVO), (incorporated herein by reference).
- The lipases of the present invention are included in the detergent composition in such an amount that the final detergent composition has a lipolytic enzyme activity of from 100 to 0.005 LU/mg preferably 25 to 0.05 LU/mg of the composition.
- A Lipase Unit (LU) is that amount of lipase which produces 1 micromol of titratable fatty acid per minute in a pH stat. under the following conditions: temperature 30°C; pH = 9.0; substrate is an emulsion of 3.3 wt.% of olive oil and 3.3% gum arabic, in the presence of 13 mmol/l Ca²⁺ and 20 mmol/l NaCl in 5 mmol/l Tris-buffer.
- Naturally, mixtures of the above lipases can be used. The lipases can be used in their nonpurified form, or in a purified form, e.g. purified with the aid of well-known adsorption methods, such as a phenylsepharose-adsorption techniques.
- The compositions further comprise a chlorine-type bleaching agent, generally in an amount corresponding to 0.1-15%, usually 0.5-10% by weight of available chlorine.
- By chlorine-type bleaching agents, organic and/or inorganic compounds are meant, which yield, on solution in water, active chlorine. Typical examples are alkali metal hypochlorites, chlorinated trisodium phosphate, chlorinated (sulphon) amides, chlorinated hydantoins, chlorinated cyanuric acids and salts (usually alkali metal, e.g. sodium, salts) thereof, etc.
- The compositions also contain a detergent-active compound, generally in an amount of from 0.5-10%, usually 1-5%. Any well-known type of detergent active compound may be used, such as soaps, synthetic anionic, non-ionic, amphoteric detergent surfactant and mixtures thereof. Preferably, a nonionic detergent surfactant is used, especially a low-foaming one. Suitable examples of such nonionic detergent surfactants can easily be found in M Schick "Nonionic Surfactants" (1967).
- The composition of the invention may furthermore comprise the usual ingredients of dishwashing or rinse compositions. Thus it may contain one or more alkali salts commonly used in dishwashing compositions. Thus, it may contain organic and/or inorganic builders such as the alkali metal ortho-, pyro and tripolyphosphates and hexametaphosphates, silicates, carbonates, zeolites, borates, citrates, carboxymethyloxysuccinates, nitrilotriacetates and ethylenediamine-tetraacetates, polymeric polyelectrolytes such as polyacrylates, polymaleates, and other known organic and inorganic builder compounds.
- Caustic alkali (e.g. NAOH) may also be additionally present, and the compositions often generate a pH >10 on dissolution/dispersion at a surfactant level in the range of 0.4 - 0.8 g/l.
- Usually, the amount of builders in the composition varies from 10-90% by weight, generally from 30-70% by weight.
- The composition may furthermore contain other useful additives such as oxygen-type bleaching agents such as perborate, reducing bleaching agents such as sodium sulphite, bleaching agent activators, hydrotropes, fillers, perfumes, colouring agents, germicides, soil-suspending agents, aminopoly-phosphonic acids and alkali metal or alkaline earth metal salts thereof, clays such as hectorites, anti-corrosion agents such as fatty acids, benztriazole and so on. Other enzymes such as proteases, e.g. Savinase R ex Novo, amylases, e.g. Termamyl R ex Novo, and oxidases may also be included.
- In general, the dishwashing compositions of the invention (preferably those in solid e.g. powder or granulate form) may contain proteases in such an amount, that the final composition has a proteolytic activity of 0.1-50, usually 1-50 and preferably 5-30 GU/mg. A GU is a glycine unit, which is the amount of enzyme which under standard incubation conditions produces an amount of terminal NH₂-groups equivalent to 1 microgram/ml glycine.
- It is explained that the preferred proteases are those of the subtilisen type (e.g. the Savinase preparation mentioned above), but it is preferred that the lipase preparation is itself substantially free of accompanying protease, e.g. less than about 0.3 GU per lipase unit, preferably not more than about 0.15 GU per lipase unit.
- When amylases are present, they are used in such amounts that the final composition has an amylolytic activity of 10³-10⁷ MU/kg of final product. A maltose unit (MU) is determined by the method as described in P Bernfeld in "Methods in Enzymology", Vol I, (1955), page 149.
- A typical example of a machine dishwashing composition contains a lipase in an amount as set out above, an alkali metal tripolyphosphate in an amount of from 20-60%, an alkali metal silicate in an amount of from 40-80%, or an alkali metal disilicate in an amount of 5-30% by weight, a chlorine-type bleaching agent such as dichlorocyanuric acid (sodium or potassium salt) in an amount of from 0.5-10%, a low-foaming detergent surfactant in an amount of from 0.5-5%, and minor ingredients such as perfumes, colouring agents, hydrotropes, fillers, etc.
- The products of the invention can be formulated in any desirable form, such as powders, granulates, cakes, bars, pastes, liquids etc. When the compositions are presented as liquids, the proportions given above are (wherever appropriate) expressed in terms of the dry weight.
- The invention will further be illustrated by way of example.
- The following formulations were made:
A B C (% by weight) Granular sodium tripolyphosphate (7% water of hydration) 36.0 38.7 35.0 Sodium metasilicate (0.aq) - 16.5 - Sodium metasilicate (5.aq) - - 7.0 Granular sodium metasilicate - - 55.0 (18% water of hydration) Sodium disilicate 11.0 - - Sodium carbonate 9.0 - - C₁₃-C₁₅ linear alcohol, condensed with 2 moles of ethylene oxide and 4 moles of propylene oxide - - 1.0 C₁₂-C₁₅ near alcohol, condensed with 4.4 moles of ethylene oxide and 6.5 moles of propylene oxide 1.4 1.0 - Sodium sulphate 22.0 34.0 - Sodium dichlorocyanuric acid salt (2.aq) 1.2 1.2 1.2 Water to 100.0 100.0 100.0 - Solutions were made of 3 g/l of each of these formulations in water of 9° German hardness at 30°C and Lipolase was added in an amount of 15 LU/ml. The residual activity was measured after 25 minutes storage. The following results were obtained:
residual activity (in %) A 60 B 65 C 35 - With composition B of Example 1, the same test was repeated (at pH 10.9) with Lipolase, or the lipase ex Pseudomonas cepacia or the lipase ex Humicola lanuginosa according to European Patent Application 0 258 068, all dosed at 15 LU/ml.
- The following results were obtained, showing that all three lipases retained a useful degree of activity, the preferred lipase being the Lipolase preparation.
residual activity (in %) Lipolase 65 Pseudomonas cepacia 10 Humicola lanuginosa 10 - In relation to the above result, it is believed that the lipolase enzyme (highly preferred) is free of protease of fungal origin, while the Lipase obtained directly from Humicola lanuginosa had some fungal protease therein, (probably more than 0.3 GU per Lipase unit).
- Repeating this test, using formulation B, in which, however, the sodium dichlorocyanuric acid salt was replaced by sodium hypochlorite (to yield 154 mg/l Na0Cl solution), the following results were obtained:
residual activity (in %) Lipolase 65 Pseudomonas cepacia 20 - Glasses were cleaned in a Kenmore Sears dishwashing machine, using the normal wash programme at 50°C followed by a hot dry. The water hardness was 14° FH. The dishwashing composition was dosed in an amount of 3 g/l, and had the following formulation:
% by weight sodium tripolyphosphate 24.0 soda ash 20.0 sodium disilicate 11.0 linear C₁₀ alcohol, condensed with 6 moles of ethylene oxide and 24 moles of propylene oxide 2.5 sodium sulphate 44.0 sodium dichlorocyanuric acid salt 1.2 water to 100.0 - The load was a dummy load without soil, and the soiling was 35 g/run fresh egg-yolk.
- The glasses were washed once and the number of spots on the glasses was thereafter determined. These experiments were carried out with and without Lipolase (dosed at 15 LU/ml), with or without Savinase (dosed at 47 GU/ml).
- The following results were obtained:
Number of spots on glass Base powder without chlorine bleach 281 powder with chlorine bleach 298 powder with chlorine bleach + Lipolase 36 powder with chlorine bleach + Savinase 330 powder with chlorine bleach + Lipolase + Savinase 38 - The invention extends to all combinations and subcombinations of the features mentioned above and in the appended claims, within the scope of the claims.
Claims (6)
- A dishwashing or rinsing composition comprising a surfactant, a chlorine-type bleaching agent in a non-protected form and a lipolytic enzyme in an amount in the range 0.005 to 100 lipase units per mg (dry weight) of the composition, whereby the lipolytic enzyme is selected from lipases which show a positive immunological cross-reaction with antibody raised against lipase from Chromobacter viscosum var. lipolyticum NRRL B-3673 and lipases which show a positive such reaction with antibody raised against lipase from Humicola lanuginosa (syn. Thermomyces lanuginosus).
- A composition according to Claim 1, characterised in that the chlorine-type bleaching agent is selected from alkali metal hypochlorites, chlorinated trisodium phosphate, chlorinated sulphonamides, chlorinated hydantoins, chlorinated cyanuric acids and salts thereof.
- A composition according to claim 1, characterised in that on dissolution or dispersion at a surfactant level in the range of 0.4 - 0.8 g/l it generates a pH of more than 10, and comprises sodium silicate or other alkali salt, optionally with added caustic alkali.
- A composition according to claim 1, characterised in that it further comprises a subtilisin protease enzyme in an amount in the range 0.1 - 50 GU/mg.
- A composition according to claim 1, characterised in that the lipase enzyme is Lipolase (TM).
- A process of (e.g. mechanical) dishwashing, characterised by the use of a dishwashing or rinsing composition according to claim 1.
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
GB888813688A GB8813688D0 (en) | 1988-06-09 | 1988-06-09 | Enzymatic dishwashing composition |
GB8813688 | 1988-06-09 |
Publications (2)
Publication Number | Publication Date |
---|---|
EP0346137A1 EP0346137A1 (en) | 1989-12-13 |
EP0346137B1 true EP0346137B1 (en) | 1995-10-04 |
Family
ID=10638372
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
EP89305836A Expired - Lifetime EP0346137B1 (en) | 1988-06-09 | 1989-06-09 | Enzymatic dishwashing composition |
Country Status (12)
Country | Link |
---|---|
US (1) | US5112518A (en) |
EP (1) | EP0346137B1 (en) |
JP (1) | JPH02504648A (en) |
AU (1) | AU616780B2 (en) |
BR (1) | BR8907008A (en) |
CA (1) | CA1335969C (en) |
DE (1) | DE68924444T2 (en) |
ES (1) | ES2079378T3 (en) |
GB (1) | GB8813688D0 (en) |
NO (1) | NO174516B (en) |
WO (1) | WO1989012089A1 (en) |
ZA (1) | ZA894391B (en) |
Families Citing this family (21)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
GB8813687D0 (en) * | 1988-06-09 | 1988-07-13 | Unilever Plc | Enzymatic dishwashing & rinsing composition |
GB2247025A (en) * | 1990-08-13 | 1992-02-19 | Unilever Plc | Enzymatic dishwashing and rinsing composition |
US5733473A (en) * | 1990-11-14 | 1998-03-31 | The Procter & Gamble Company | Liquid detergent composition containing lipase and protease |
US5474699A (en) * | 1991-05-31 | 1995-12-12 | Colgate-Palmolive Co. | Phosphate containing powered automatic dishwashing composition with enzymes |
US5693602A (en) * | 1991-05-31 | 1997-12-02 | Colgate-Palmolive Co. | Spray dried powered automatic dishwashing composition containing enzymes |
WO1994025557A1 (en) * | 1993-04-27 | 1994-11-10 | The Procter & Gamble Company | Liquid or granular automatic dishwashing detergent compositions |
WO1994025556A1 (en) * | 1993-04-27 | 1994-11-10 | The Procter & Gamble Company | Liquid or granular automatic dishwashing detergent compositions |
TR28788A (en) * | 1993-05-25 | 1997-03-25 | Henkel Ecolab Gmbh & Co Ohg | Methods and equipment for machine-dishwashing cleaning. |
AU7719194A (en) * | 1993-09-14 | 1995-04-03 | Procter & Gamble Company, The | Machine dishwashing composition comprising lipolytic and proteolytic enzymes |
WO1995007980A1 (en) * | 1993-09-14 | 1995-03-23 | The Procter & Gamble Company | Manual dishwashing composition comprising amylase and lipase enzymes |
US5510052A (en) * | 1994-08-25 | 1996-04-23 | Colgate-Palmolive Co. | Enzymatic aqueous pretreatment composition for dishware |
EP0994936A1 (en) * | 1997-07-02 | 2000-04-26 | The Procter & Gamble Company | Dishwashing compositions comprising a phospholipase and an amylase |
US5958855A (en) * | 1998-03-20 | 1999-09-28 | Colgate Palmolive Company | Powdered automatic dishwashing tablets |
US6191088B1 (en) * | 1998-03-20 | 2001-02-20 | Colgate-Palmolive Co. | Powdered automatic dishwashing composition |
WO2003028869A2 (en) * | 2001-10-03 | 2003-04-10 | Levtech, Inc. | Mixing bag or vessel having a receiver for a fluid-agitating element |
EP2428572A3 (en) | 2007-03-09 | 2012-12-12 | Danisco US, Inc., Genencor Division | Alkaliphilic Bacillus species alpha-amylase variants, compositions comprising alpha-amylase variants, and methods of use |
MX2010013123A (en) | 2008-06-06 | 2011-01-14 | Danisco Inc | Variant alpha-amylases from bacillus subtilis and methods of use, thereof. |
CA2726630A1 (en) | 2008-06-06 | 2009-12-10 | Danisco Us Inc. | Production of glucose from starch using alpha-amylases from bacillus subtilis |
WO2009149283A1 (en) | 2008-06-06 | 2009-12-10 | Danisco Us Inc. | Saccharification enzyme composition |
CA2738447C (en) | 2008-09-25 | 2019-01-08 | Danisco Us Inc. | Alpha-amylase blends and methods for using said blends |
EP2491121A2 (en) | 2009-10-23 | 2012-08-29 | Danisco US Inc. | Methods for reducing blue saccharide |
Family Cites Families (13)
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---|---|---|---|---|
GB1238692A (en) * | 1967-06-01 | 1971-07-07 | ||
US3817869A (en) * | 1972-08-17 | 1974-06-18 | Procter & Gamble | Dishwasher detergent composition |
US3816320A (en) * | 1972-11-24 | 1974-06-11 | Fmc Corp | Stable dishwashing compositions containing sodium dichloroisocyanurate dihydrate |
CH651314A5 (en) * | 1981-12-23 | 1985-09-13 | Colgate Palmolive Co | DETERGENT COMPOSITION FOR DISHWASHER. |
US4421664A (en) * | 1982-06-18 | 1983-12-20 | Economics Laboratory, Inc. | Compatible enzyme and oxidant bleaches containing cleaning composition |
GB8514708D0 (en) * | 1985-06-11 | 1985-07-10 | Unilever Plc | Enzymatic detergent composition |
GB8514707D0 (en) * | 1985-06-11 | 1985-07-10 | Unilever Plc | Enzymatic detergent composition |
DE3750450T2 (en) * | 1986-08-29 | 1995-01-05 | Novo Industri As | Enzyme-based detergent additive. |
GB8624050D0 (en) * | 1986-10-07 | 1986-11-12 | Unilever Plc | Machine dishwashing compositions |
GB8629538D0 (en) * | 1986-12-10 | 1987-01-21 | Unilever Plc | Enzymatic dishwashing & rinsing composition |
GB8629534D0 (en) * | 1986-12-10 | 1987-01-21 | Unilever Plc | Enzymatic detergent & bleaching composition |
US4959179A (en) * | 1989-01-30 | 1990-09-25 | Lever Brothers Company | Stabilized enzymes liquid detergent composition containing lipase and protease |
US4908150A (en) * | 1989-02-02 | 1990-03-13 | Lever Brothers Company | Stabilized lipolytic enzyme-containing liquid detergent composition |
-
1988
- 1988-06-09 GB GB888813688A patent/GB8813688D0/en active Pending
-
1989
- 1989-06-08 CA CA000602203A patent/CA1335969C/en not_active Expired - Fee Related
- 1989-06-09 WO PCT/GB1989/000649 patent/WO1989012089A1/en unknown
- 1989-06-09 ES ES89305836T patent/ES2079378T3/en not_active Expired - Lifetime
- 1989-06-09 EP EP89305836A patent/EP0346137B1/en not_active Expired - Lifetime
- 1989-06-09 DE DE68924444T patent/DE68924444T2/en not_active Expired - Fee Related
- 1989-06-09 JP JP89506714A patent/JPH02504648A/en active Pending
- 1989-06-09 ZA ZA894391A patent/ZA894391B/en unknown
- 1989-06-09 AU AU37698/89A patent/AU616780B2/en not_active Ceased
- 1989-06-09 BR BR898907008A patent/BR8907008A/en not_active Application Discontinuation
- 1989-12-08 US US07/449,134 patent/US5112518A/en not_active Expired - Fee Related
-
1990
- 1990-02-08 NO NO900607A patent/NO174516B/en unknown
Also Published As
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---|---|
NO174516C (en) | 1994-05-18 |
DE68924444T2 (en) | 1996-03-21 |
JPH02504648A (en) | 1990-12-27 |
NO900607D0 (en) | 1990-02-08 |
ZA894391B (en) | 1991-02-27 |
AU616780B2 (en) | 1991-11-07 |
GB8813688D0 (en) | 1988-07-13 |
AU3769889A (en) | 1990-01-05 |
ES2079378T3 (en) | 1996-01-16 |
NO174516B (en) | 1994-02-07 |
CA1335969C (en) | 1995-06-20 |
BR8907008A (en) | 1990-12-26 |
NO900607L (en) | 1990-02-08 |
US5112518A (en) | 1992-05-12 |
WO1989012089A1 (en) | 1989-12-14 |
DE68924444D1 (en) | 1995-11-09 |
EP0346137A1 (en) | 1989-12-13 |
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